Creatine kinase shapes up

Article Abstract:

The crystal structure of creatine kinases (CKs), which are a family of distinct but related enzymes, has two different NaATP binding sites in two distinct crystal forms. The nucleotide binding is present in the central region of the monomer and ATP is bound with the adenine base in the anti orientation relative to ribose. CKs are mostly present in rapidly respiring tissues of vertebrates. The use of octameric mitochondrial (Mi(sub b))-CK from chicken cardiac tissue enables the study of CK crystal structure.

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Structure of mitochondrial creatine kinase

Article Abstract:

The structure of an octameric mitochondrial isoform of creatine kinase has 422 point-group symmetry. It has a cube-like appearance of side length 93 angstroms with a channel 20 angstroms wide extending along the four-fold axis. The kinase is located in the intermembrane compartment and along the cristae membranes. A small alpha-helical domain and a large domain of eight-stranded antiparallel beta-sheet flanked by seven alpha-helices exist in each monomer.

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A non-receptor tyrosine kinase that inhibits the GTPase activity of p21 (supercdc42)

Article Abstract:

A hippocampal complementary DNA encoding a tyrosine kinase binds Cdc42Hs in its GTP-bound form. A unique sequence of 47 amino acids, C-terminal to an SH3 domain, mediates this binding. It also inhibits both the intrinsic and GAP-stimulated GTPase activity of Cdc42Hs. A regulatory mechanism may be sustaining the GTP-bound active form of cdc42Hs and a tyrosine phosphorylation pathway is linked directly to it.

Analysis, Protein tyrosine kinase, Protein-tyrosine kinase

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